2zp2

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[[Image:2zp2.png|left|200px]]
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==C-terminal domain of KipI from Bacillus subtilis==
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<StructureSection load='2zp2' size='340' side='right' caption='[[2zp2]], [[Resolution|resolution]] 3.01&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2zp2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZP2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZP2 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">kipI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zp2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zp2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zp2 RCSB], [http://www.ebi.ac.uk/pdbsum/2zp2 PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zp/2zp2_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The sensor histidine kinase A (KinA) from Bacillus subtilis triggers a phosphorelay that activates sporulation. The antikinase KipI prevents sporulation by binding KinA and inhibiting the autophosphorylation reaction. Using neutron contrast variation, mutagenesis, and fluorescence data, we show that two KipI monomers bind via their C-domains at a conserved proline in the KinA dimerization and histidine-phosphotransfer (DHp) domain. Our crystal structure of the KipI C-domain reveals the binding motif has a distinctive hydrophobic groove formed by a five-stranded antiparallel beta-sheet; a characteristic of the cyclophilin family of proteins that bind prolines and often act as cis-trans peptidyl-prolyl isomerases. We propose that the DHp domain of KinA transmits conformational signals to regulate kinase activity via this proline-mediated interaction. Given that both KinA and KipI homologues are widespread in the bacterial kingdom, this mechanism has broad significance in bacterial signal transduction.
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{{STRUCTURE_2zp2| PDB=2zp2 | SCENE= }}
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Histidine kinase regulation by a cyclophilin-like inhibitor.,Jacques DA, Langley DB, Jeffries CM, Cunningham KA, Burkholder WF, Guss JM, Trewhella J J Mol Biol. 2008 Dec 12;384(2):422-35. Epub 2008 Sep 16. PMID:18823995<ref>PMID:18823995</ref>
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===C-terminal domain of KipI from Bacillus subtilis===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_18823995}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[2zp2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZP2 OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:018823995</ref><references group="xtra"/>
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[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Jacques, D A.]]
[[Category: Jacques, D A.]]

Revision as of 05:25, 2 October 2014

C-terminal domain of KipI from Bacillus subtilis

2zp2, resolution 3.01Å

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